Article

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain

2023-07-10

Abstract excerpt

Mutations in the tyrosine phosphatase SHP2 are associated with a variety of human diseases. Most mutations in SHP2 increase its basal catalytic activity by disrupting auto-inhibitory interactions between its phosphatase domain and N-terminal SH2 (phosphotyrosine recognition) domain. By contrast, some disease-associated mutations located in the ligand-binding pockets of the N- or C- terminal SH2 domains do not incr...

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Literature Corpus work: f277062a-d4eb-5744-af53-50c78a510561
DOI: 10.1101/2023.07.10.548257

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